Thialysine- and selenalysine-resistance in a E. coli mutant
Affiliations
- PMID: 3149757
Item in Clipboard
Thialysine- and selenalysine-resistance in a E. coli mutant
Physiol Chem Phys Med NMR.
1988.
Abstract
A thialysine-resistant mutant of E. coli strain KL16 also shows a lower sensitivity to selenalysine, the lysine analog containing selenium. No difference between the mutant and the parental strain has been shown regarding the affinities of the transport systems and the lysyl-tRNA synthetase for selenalysine, thialysine and lysine as well as the inhibitory effects of these three aminoacids on the activity of the lysine biosynthetic pathway. A marked difference between the two strains has been evidenced in the AK III repression: in the mutant the repression by selenalysine, thialysine and lysine is much lower than in the parental strain.
Similar articles
-
Aspartokinase III repression in a thialysine-resistant mutant of E. coli.Biochem Int. 1988 Sep;17(3):545-54. Biochem Int. 1988. PMID: 2849443
-
Aspartokinase III repression and lysine analogs utilization for protein synthesis.Physiol Chem Phys Med NMR. 1990;22(4):241-5. Physiol Chem Phys Med NMR. 1990. PMID: 2129308
-
Isolation of thialysine--and selenalysine--resistant mutants of E. coli and CHO cells.Ital J Biochem. 1989 Jul-Aug;38(4):271A-273A. Ital J Biochem. 1989. PMID: 2511161 No abstract available.
-
Regulation of lysine biosynthesis in Escherichia coli K12.Acta Microbiol Acad Sci Hung. 1976;23(2):121-8. Acta Microbiol Acad Sci Hung. 1976. PMID: 9781 Review.
-
Production of transgenic plants containing elevated levels of lysine and threonine.Biochem Soc Trans. 1994 Nov;22(4):921-5. doi: 10.1042/bst0220921. Biochem Soc Trans. 1994. PMID: 7698485 Review. No abstract available.